ID A0A0N1F9U0_9PROT Unreviewed; 467 AA.
AC A0A0N1F9U0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
GN ORFNames=GLUCOINTEAF2_0200429 {ECO:0000313|EMBL:KPH87559.1};
OS Komagataeibacter intermedius AF2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=1458464 {ECO:0000313|EMBL:KPH87559.1, ECO:0000313|Proteomes:UP000031553};
RN [1] {ECO:0000313|EMBL:KPH87559.1, ECO:0000313|Proteomes:UP000031553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF2 {ECO:0000313|EMBL:KPH87559.1,
RC ECO:0000313|Proteomes:UP000031553};
RA Santos R.A., Berretta A.A., Barud H.S., Ribeiro S.J., Gonzalez-Garcia L.N.,
RA Zucchi T.D., Goldman G.H., Riano-Pachon D.M.;
RT "Draft Genome Sequence of Komagataeibacter intermedius Strain AF2, Isolated
RT from Kombucha Tea.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000256|RuleBase:RU363071};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC manganese, cobalt or cadmium ions. {ECO:0000256|PIRSR:PIRSR602480-1};
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPH87559.1}.
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DR EMBL; JUFX02000112; KPH87559.1; -; Genomic_DNA.
DR RefSeq; WP_039735557.1; NZ_JUFX02000112.1.
DR AlphaFoldDB; A0A0N1F9U0; -.
DR OrthoDB; 9766852at2; -.
DR Proteomes; UP000031553; Unassembled WGS sequence.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR NCBIfam; TIGR01358; DAHP_synth_II; 1.
DR PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cadmium {ECO:0000256|PIRSR:PIRSR602480-1};
KW Cobalt {ECO:0000256|PIRSR:PIRSR602480-1};
KW Manganese {ECO:0000256|PIRSR:PIRSR602480-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 118
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 301
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 406
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 467 AA; 51739 MW; F306FF7DC2EBE2B9 CRC64;
MSATHSHNSS SRQAWTPESW RSFPARQMPR YPDEAALQGV EARLRRYPPL VFAGEARRLR
AHLAKAATGQ AFVLQGGACA ESFSEFTADI VRDTFRVLLQ MAVVLTFGAK VPVIKIGRMA
GQYAKPRSSD TETKDGVTLP SYRGDIINGS DFTEAARIPD PKRMETGYFQ SVGTMNLLRA
FAGGGYANLH EVHRWNLGFV ERSPLAQRYG QLAERIGETL DFMAACGLTA ATTPQIDETE
FYTSHEALLL PYEQALTRID STSDEWYDCS AHFVWIGDRT RQPDGAHVEF LRGVRNPIGI
KVGPTTTIED LEQLLDILNP TDEAGRISLI SRMGAGKVRE HLPPLLEKVM ATGRTVTWLC
DPMHGNTSST STGVKTRSFD AILSEIHGFF DVFEAAGAHP GGVHFEMTGQ NVTECIGGAH
RLTEDDLGER YETFCDPRLN AEQSLEMAFR LAEELKTRMH RMHGGAR
//
